Pub. Date : 2006 Nov 10
PMID : 16980304
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Mutational analysis of Bcl-2 further showed that the two cysteine residues of Bcl-2 (Cys158 and Cys229) are important in the S-nitrosylation process and that mutations of these cysteines completely inhibited Bcl-2 S-nitrosylation. | Cysteine | BCL2 apoptosis regulator | Homo sapiens |
2 | Mutational analysis of Bcl-2 further showed that the two cysteine residues of Bcl-2 (Cys158 and Cys229) are important in the S-nitrosylation process and that mutations of these cysteines completely inhibited Bcl-2 S-nitrosylation. | Cysteine | BCL2 apoptosis regulator | Homo sapiens |
3 | Mutational analysis of Bcl-2 further showed that the two cysteine residues of Bcl-2 (Cys158 and Cys229) are important in the S-nitrosylation process and that mutations of these cysteines completely inhibited Bcl-2 S-nitrosylation. | Cysteine | BCL2 apoptosis regulator | Homo sapiens |
4 | Mutational analysis of Bcl-2 further showed that the two cysteine residues of Bcl-2 (Cys158 and Cys229) are important in the S-nitrosylation process and that mutations of these cysteines completely inhibited Bcl-2 S-nitrosylation. | Cysteine | BCL2 apoptosis regulator | Homo sapiens |
5 | Mutational analysis of Bcl-2 further showed that the two cysteine residues of Bcl-2 (Cys158 and Cys229) are important in the S-nitrosylation process and that mutations of these cysteines completely inhibited Bcl-2 S-nitrosylation. | Cysteine | BCL2 apoptosis regulator | Homo sapiens |
6 | Mutational analysis of Bcl-2 further showed that the two cysteine residues of Bcl-2 (Cys158 and Cys229) are important in the S-nitrosylation process and that mutations of these cysteines completely inhibited Bcl-2 S-nitrosylation. | Cysteine | BCL2 apoptosis regulator | Homo sapiens |